| Tag | Content |
|---|
| CPLM ID | CPLM-004970 |
UniProt Accession | |
Genbank Protein ID | |
Genbank Nucleotide ID | |
Protein Name | Cyclic di-GMP phosphodiesterase YahA |
Protein Synonyms/Alias | |
Gene Name | yahA |
Gene Synonyms/Alias | b0315; JW0307 |
Created Date | July 27, 2013 |
Organism | Escherichia coli (strain K12) |
NCBI Taxa ID | 83333 |
Lysine Modification | Position | Peptide | Type | References |
|---|
| 28 | LPGSVSEKERLLLKL | acetylation | [1] | | 221 | ECLNLVNKLGNDKIK | acetylation | [1] | | 351 | SPPVPGNKFISEWVM | acetylation | [1] |
|
Reference | [1] Acetyl-Phosphate Is a Critical Determinant of Lysine Acetylation in E. coli. Weinert BT, Iesmantavicius V, Wagner SA, Schölz C, Gummesson B, Beli P, Nyström T, Choudhary C. Mol Cell. 2013 Jul 25;51(2):265-72. [ PMID: 23830618] |
Functional Description | Hydrolyzes c-di-GMP (cyclic bis(3'-5') dimeric GMP) to 5'-pGpG, known as PDE-A activity. PDE-B activity, that is hydrolysis of 5'-pGpG to GMP, proceeds only very slowly. |
Sequence Annotation | DOMAIN 18 83 HTH luxR-type.
DOMAIN 106 360 EAL. |
Keyword | c-di-GMP; Complete proteome; DNA-binding; Hydrolase; Magnesium; Manganese; Reference proteome. |
Sequence Source | UniProt (SWISSPROT/TrEMBL); GenBank; EMBL |
Protein Length | 362 AA |
Protein Sequence | MNSCDFRVFL QEFGTTVHLS LPGSVSEKER LLLKLLMQGM SVTEISQYRN RSAKTISHQK 60
KQLFEKLGIQ SDITFWRDIF FQYNPEIISA TGSNSHRYIN DNHYHHIVTP EAISLALENH 120
EFKPWIQPVF CAQTGVLTGC EVLVRWEHPQ TGIIPPDQFI PLAESSGLIV IMTRQLMKQT 180
ADILMPVKHL LPDNFHIGIN VSAGCFLAAG FEKECLNLVN KLGNDKIKLV LELTERNPIP 240
VTPEARAIFD SLHQHNITFA LDDFGTGYAT YRYLQAFPVD FIKIDKSFVQ MASVDEISGH 300
IVDNIVELAR KPGLSIVAEG VETQEQADLM IGKGVHFLQG YLYSPPVPGN KFISEWVMKA 360
GG 362 |
Gene Ontology | GO:0005622; C:intracellular; IEA:InterPro. GO:0071111; F:cyclic-guanylate-specific phosphodiesterase activity; IDA:EcoCyc. GO:0043565; F:sequence-specific DNA binding; IEA:InterPro. GO:0003700; F:sequence-specific DNA binding transcription factor activity; IEA:InterPro. |
Interpro | |
Pfam | |
SMART | |
PROSITE | |
PRINTS | |